HSP70 anticorps (AA 365-681)

N° du produit ABIN361730

Cet anticorps Lapin Polyclonal détecte spécifiquement HSP70 dans WB, IF et ICC. Il présente une réactivité envers Plasmodium falciparum et a été mentionné dans 7+ publications.

Aperçu rapide pour HSP70 anticorps (AA 365-681) (ABIN361730)

Antigène: HSP70 (Heat Shock Protein 70 (HSP70))

Reactivité: Plasmodium falciparum

Hôte: Lapin

Clonalité: Polyclonal

Conjugué: Cet anticorp HSP70 est non-conjugé

Application: Western Blotting (WB), Immunofluorescence (IF), Immunocytochemistry (ICC)

Détail du produit anti-HSP70 anticorps

Épitope: AA 365-681

Specificité: Detects ~ 70 kDa. Specific to P. falciparum and does not cross-react to any protein from Human erythrocytes.

Réactivité croisée: Plasmodium falciparum

Purification: Protein A Purified

Immunogène: His-tagged and purified PfHSP70, C-terminus (AA 365-681)

Information d'application

Indications d'application:

• WB (1:2000)
• ICC/IF (1:50)
• optimal dilutions for assays should be determined by the user.

Commentaires:

0.15 μg/ml of ABIN361729 was sufficient for detection of PfHSP70 in 20 μg of P. falciparum lysate by colorimetric immunoblot analysis using Goat anti-rabbit IgG:HRP as the secondary antibody.

Restrictions: For Research Use only

Stockage

Format: Liquid

Concentration: 1 mg/mL

Buffer: PBS pH 7.4, 50 % glycerol, 0.09 % sodium azide, Storage buffer may change when conjugated

Agent conservateur: Sodium azide

Précaution d'utilisation: This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.

Stock: -20 °C

Stockage commentaire: -20°C

Références pour anticorps anti-HSP70 (ABIN361730)

Llorà-Batlle, Michel-Todó, Witmer, Toda, Fernández-Becerra, Baum, Cortés: "Conditional expression of PfAP2-G for controlled massive sexual conversion in Plasmodium falciparum." dans: Science advances, Vol. 6, Issue 24, pp. eaaz5057, (2020) (PubMed).

Bancells, Llorà-Batlle, Poran, Nötzel, Rovira-Graells, Elemento, Kafsack, Cortés: "Revisiting the initial steps of sexual development in the malaria parasite Plasmodium falciparum." dans: Nature microbiology, Vol. 4, Issue 1, pp. 144-154, (2019) (PubMed).

Hallée, Boddey, Cowman, Richard: "Evidence that the Plasmodium falciparum Protein Sortilin Potentially Acts as an Escorter for the Trafficking of the Rhoptry-Associated Membrane Antigen to the Rhoptries." dans: mSphere, Vol. 3, Issue 1, (2018) (PubMed).

Hallée, Richard: "Evidence that the Malaria Parasite Plasmodium falciparum Putative Rhoptry Protein 2 Localizes to the Golgi Apparatus throughout the Erythrocytic Cycle." dans: PLoS ONE, Vol. 10, Issue 9, pp. e0138626, (2016) (PubMed).

Goel, Palmkvist, Moll, Joannin, Lara, Akhouri, Moradi, Öjemalm, Westman, Angeletti, Kjellin, Lehtiö, Blixt, Ideström, Gahmberg, Storry, Hult, Olsson, von Heijne, Nilsson, Wahlgren: "RIFINs are adhesins implicated in severe Plasmodium falciparum malaria." dans: Nature medicine, Vol. 21, Issue 4, pp. 314-7, (2015) (PubMed).

Boes, Spiegel, Voepel, Edgue, Beiss, Kapelski, Fendel, Scheuermayer, Pradel, Bolscher, Behet, Dechering, Hermsen, Sauerwein, Schillberg, Reimann, Fischer: "Analysis of a Multi-component Multi-stage Malaria Vaccine Candidate-Tackling the Cocktail Challenge." dans: PLoS ONE, Vol. 10, Issue 7, pp. e0131456, (2015) (PubMed).

Sanz, Bandini, Ospina, Bernabeu, Mariño, Fernández-Becerra, Izquierdo: "Biosynthesis of GDP-fucose and other sugar nucleotides in the blood stages of Plasmodium falciparum." dans: The Journal of biological chemistry, Vol. 288, Issue 23, pp. 16506-17, (2013) (PubMed).

Détails sur HSP70

Antigène: HSP70 (Heat Shock Protein 70 (HSP70))

Autre désignation: HSP70

Sujet: HSP70 genes encode abundant heat-inducible 70- kDa HSPs (HSP70s). In most eukaryotes HSP70 genes exist as part of a multigene family. They are found in most cellular compartments of eukaryotes including nuclei, mitochondria, chloroplasts, the endoplasmic reticulum and the cytosol, as well as in bacteria. The genes show a high degree of conservation, having at least 5O% identity (1). The N-terminal two thirds of HSP70s are more conserved than the C-terminal third. HSP70 binds ATP with high affinity and possesses a weak ATPase activity which can be stimulated by binding to unfolded proteins and synthetic peptides (2). When HSC70 (constitutively expressed) present in mammalian cells was truncated, ATP binding activity was found to reside in an N-terminal fragment of 44 kDa which lacked peptide binding capacity. Polypeptide binding ability therefore resided within the C-terminal half (3). The structure of this ATP binding domain displays multiple features of nucleotide binding proteins (4). All HSP70s, regardless of location, bind proteins, particularly unfolded ones. The molecular chaperones of the HSP70 family recognize and bind to nascent polypeptide chains as well as partially folded intermediates of proteins preventing their aggregation and misfolding. The binding of ATP triggers a critical conformational change leading to the release of the bound substrate protein (5). The universal ability of HSP70s to undergo cycles of binding to and release from hydrophobic stretches of partially unfolded proteins determines their role in a great variety of vital intracellular functions such as protein synthesis, protein folding and oligomerization and protein transport. PfHSP70-I (PF08_0054) is the major cytosolic HSP70 in Plasmodium falciparum. It is abundantly expressed in the blood stages of the parasite and is thought to constitute 1-2 % of total parasite protein. It is induced upon heat shock. It is present in the parasite in different complexes with PfHSP90 and some PfHSP40 (6, 7). Looking for more information on HSP70? Visit our new HSP70 Scientific Resource Guide at http://www.HSP70.com.

UniProt: P11144